ID   HEPC_HUMAN              Reviewed;          84 AA.
AC   P81172; Q1HE14; Q9BY68;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Hepcidin {ECO:0000305};
DE   AltName: Full=Liver-expressed antimicrobial peptide 1;
DE            Short=LEAP-1;
DE   AltName: Full=Putative liver tumor regressor;
DE            Short=PLTR;
DE   Contains:
DE     RecName: Full=Hepcidin-25;
DE              Short=Hepc25;
DE   Contains:
DE     RecName: Full=Hepcidin-20;
DE              Short=Hepc20;
DE   Flags: Precursor;
GN   Name=HAMP {ECO:0000312|HGNC:HGNC:15598}; Synonyms=HEPC, LEAP1;
GN   ORFNames=UNQ487/PRO1003;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 60-84.
RC   TISSUE=Liver, and Urine;
RX   PubMed=11113131; DOI=10.1074/jbc.m008922200;
RA   Park C.H., Valore E.V., Waring A.J., Ganz T.;
RT   "Hepcidin: a urinary antimicrobial peptide synthesized in the liver.";
RL   J. Biol. Chem. 276:7806-7810(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 60-84, TISSUE SPECIFICITY,
RP   MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Blood, and Liver;
RX   PubMed=11034317; DOI=10.1016/s0014-5793(00)01920-7;
RA   Krause A., Neitz S., Maegert H.-J., Schulz A., Forssmann W.-G.,
RA   Schulz-Knappe P., Adermann K.;
RT   "LEAP-1, a novel highly disulfide-bonded human peptide exhibits
RT   antimicrobial activity.";
RL   FEBS Lett. 480:147-150(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Jung J.-W., Shin W.-S., Yoon Y., Lee S.-T.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   SYNTHESIS OF 60-84.
RX   PubMed=12010514; DOI=10.1034/j.1399-3011.2002.00980.x;
RA   Kluever E., Schulz A., Forssmann W.-G., Adermann K.;
RT   "Chemical synthesis of beta-defensins and LEAP-1/hepcidin.";
RL   J. Pept. Res. 59:241-248(2002).
RN   [9]
RP   INDUCTION BY LPS, AND TISSUE SPECIFICITY.
RX   PubMed=15124018; DOI=10.1172/jci20945;
RA   Nemeth E., Rivera S., Gabayan V., Keller C., Taudorf S., Pedersen B.K.,
RA   Ganz T.;
RT   "IL-6 mediates hypoferremia of inflammation by inducing the synthesis of
RT   the iron regulatory hormone hepcidin.";
RL   J. Clin. Invest. 113:1271-1276(2004).
RN   [10]
RP   REVIEW.
RX   PubMed=22306005; DOI=10.1016/j.bbamcr.2012.01.014;
RA   Ganz T., Nemeth E.;
RT   "Hepcidin and iron homeostasis.";
RL   Biochim. Biophys. Acta 1823:1434-1443(2012).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH SLC40A1.
RX   PubMed=22682227; DOI=10.1016/j.cmet.2012.03.018;
RA   Qiao B., Sugianto P., Fung E., Del-Castillo-Rueda A., Moran-Jimenez M.J.,
RA   Ganz T., Nemeth E.;
RT   "Hepcidin-induced endocytosis of ferroportin is dependent on ferroportin
RT   ubiquitination.";
RL   Cell Metab. 15:918-924(2012).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH SLC40A1.
RX   PubMed=29237594; DOI=10.1182/blood-2017-05-786590;
RA   Aschemeyer S., Qiao B., Stefanova D., Valore E.V., Sek A.C., Ruwe T.A.,
RA   Vieth K.R., Jung G., Casu C., Rivella S., Jormakka M., Mackenzie B.,
RA   Ganz T., Nemeth E.;
RT   "Structure-function analysis of ferroportin defines the binding site and an
RT   alternative mechanism of action of hepcidin.";
RL   Blood 131:899-910(2018).
RN   [13]
RP   STRUCTURE BY NMR OF 60-84, AND PRELIMINARY DISULFIDE BONDS.
RX   PubMed=12138110; DOI=10.1074/jbc.m205305200;
RA   Hunter H.N., Fulton D.B., Ganz T., Vogel H.J.;
RT   "The solution structure of human hepcidin, a peptide hormone with
RT   antimicrobial activity that is involved in iron uptake and hereditary
RT   hemochromatosis.";
RL   J. Biol. Chem. 277:37597-37603(2002).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 60-84, AND DISULFIDE BONDS.
RX   PubMed=19553669; DOI=10.1074/jbc.m109.017764;
RA   Jordan J.B., Poppe L., Haniu M., Arvedson T., Syed R., Li V., Kohno H.,
RA   Kim H., Schnier P.D., Harvey T.S., Miranda L.P., Cheetham J., Sasu B.J.;
RT   "Hepcidin revisited, disulfide connectivity, dynamics, and structure.";
RL   J. Biol. Chem. 284:24155-24167(2009).
RN   [15] {ECO:0007744|PDB:6WBV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.50 ANGSTROMS) OF 60-84, AND INTERACTION
RP   WITH SLC40A1.
RX   PubMed=32814342; DOI=10.1038/s41586-020-2668-z;
RA   Billesbolle C.B., Azumaya C.M., Kretsch R.C., Powers A.S., Gonen S.,
RA   Schneider S., Arvedson T., Dror R.O., Cheng Y., Manglik A.;
RT   "Structure of hepcidin-bound ferroportin reveals iron homeostatic
RT   mechanisms.";
RL   Nature 586:807-811(2020).
RN   [16]
RP   VARIANT HFE2B ASP-71.
RX   PubMed=14633868; DOI=10.1373/clinchem.2003.023440;
RA   Biasiotto G., Belloli S., Ruggeri G., Zanella I., Gerardi G., Corrado M.,
RA   Gobbi E., Albertini A., Arosio P.;
RT   "Identification of new mutations of the HFE, hepcidin, and transferrin
RT   receptor 2 genes by denaturing HPLC analysis of individuals with
RT   biochemical indications of iron overload.";
RL   Clin. Chem. 49:1981-1988(2003).
RN   [17]
RP   VARIANT HFE2B ASP-71.
RX   PubMed=12915468; DOI=10.1093/hmg/ddg225;
RA   Merryweather-Clarke A.T., Cadet E., Bomford A., Capron D., Viprakasit V.,
RA   Miller A., McHugh P.J., Chapman R.W., Pointon J.J., Wimhurst V.L.,
RA   Livesey K.J., Tanphaichitr V., Rochette J., Robson K.J.;
RT   "Digenic inheritance of mutations in HAMP and HFE results in different
RT   types of haemochromatosis.";
RL   Hum. Mol. Genet. 12:2241-2247(2003).
RN   [18]
RP   VARIANT HFE2B ARG-70.
RX   PubMed=14630809; DOI=10.1182/blood-2003-10-3390;
RA   Roetto A., Daraio F., Porporato P., Caruso R., Cox T.M., Cazzola M.,
RA   Gasparini P., Piperno A., Camaschella C.;
RT   "Screening hepcidin for mutations in juvenile hemochromatosis:
RT   identification of a new mutation (C70R).";
RL   Blood 103:2407-2409(2004).
RN   [19]
RP   VARIANTS HFE2B GLY-59 AND ASP-71.
RX   PubMed=14670915; DOI=10.1182/blood-2003-10-3366;
RA   Jacolot S., Le Gac G., Scotet V., Quere I., Mura C., Ferec C.;
RT   "HAMP as a modifier gene that increases the phenotypic expression of the
RT   HFE pC282Y homozygous genotype.";
RL   Blood 103:2835-2840(2004).
RN   [20]
RP   VARIANT HFE2B TYR-78.
RX   PubMed=15099344; DOI=10.1111/j.0009-9163.2004.00254.x;
RA   Delatycki M.B., Allen K.J., Gow P., MacFarlane J., Radomski C.,
RA   Thompson J., Hayden M.R., Goldberg Y.P., Samuels M.E.;
RT   "A homozygous HAMP mutation in a multiply consanguineous family with
RT   pseudo-dominant juvenile hemochromatosis.";
RL   Clin. Genet. 65:378-383(2004).
CC   -!- FUNCTION: Liver-produced hormone that constitutes the main circulating
CC       regulator of iron absorption and distribution across tissues. Acts by
CC       promoting endocytosis and degradation of ferroportin/SLC40A1, leading
CC       to the retention of iron in iron-exporting cells and decreased flow of
CC       iron into plasma (PubMed:22682227, PubMed:29237594, PubMed:32814342).
CC       Controls the major flows of iron into plasma: absorption of dietary
CC       iron in the intestine, recycling of iron by macrophages, which
CC       phagocytose old erythrocytes and other cells, and mobilization of
CC       stored iron from hepatocytes (PubMed:22306005).
CC       {ECO:0000269|PubMed:22306005, ECO:0000269|PubMed:22682227,
CC       ECO:0000269|PubMed:29237594, ECO:0000269|PubMed:32814342}.
CC   -!- FUNCTION: Has strong antimicrobial activity against E.coli ML35P
CC       N.cinerea and weaker against S.epidermidis, S.aureus and group b
CC       streptococcus bacteria. Active against the fungus C.albicans. No
CC       activity against P.aeruginosa (PubMed:11113131, PubMed:11034317).
CC       {ECO:0000269|PubMed:11034317, ECO:0000269|PubMed:11113131}.
CC   -!- SUBUNIT: Interacts with SLC40A1; this interaction promotes SLC40A1
CC       rapid ubiquitination. {ECO:0000269|PubMed:22682227,
CC       ECO:0000269|PubMed:29237594, ECO:0000269|PubMed:32814342}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11034317}.
CC   -!- TISSUE SPECIFICITY: Highest expression in liver and to a lesser extent
CC       in heart and brain. Low levels in lung, tonsils, salivary gland,
CC       trachea, prostate gland, adrenal gland and thyroid gland. Secreted into
CC       the urine and blood (PubMed:11034317). Expressed by hepatocytes
CC       (PubMed:15124018). {ECO:0000269|PubMed:11034317,
CC       ECO:0000269|PubMed:15124018}.
CC   -!- INDUCTION: Expression in hepatocytes is induced by LPS stimulus and the
CC       induction is mediated by IL6 (PubMed:15124018). Expression is inhibited
CC       in presence of TNF (PubMed:15124018). {ECO:0000269|PubMed:15124018}.
CC   -!- MASS SPECTROMETRY: [Hepcidin-25]: Mass=2789.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11034317};
CC   -!- DISEASE: Hemochromatosis 2B (HFE2B) [MIM:613313]: A juvenile form of
CC       hemochromatosis, a disorder of iron metabolism with excess deposition
CC       of iron in a variety of organs leading to their failure, bronze skin
CC       pigmentation, hepatic cirrhosis, arthropathy and diabetes. The most
CC       common symptoms of juvenile hemochromatosis at presentation are
CC       hypogonadism and cardiomyopathy. {ECO:0000269|PubMed:12915468,
CC       ECO:0000269|PubMed:14630809, ECO:0000269|PubMed:14633868,
CC       ECO:0000269|PubMed:14670915, ECO:0000269|PubMed:15099344}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the hepcidin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Hepcidin entry;
CC       URL="https://en.wikipedia.org/wiki/Hepcidin";
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DR   EMBL; AF309489; AAG23966.1; -; mRNA.
DR   EMBL; AJ277280; CAC09419.1; -; mRNA.
DR   EMBL; AF131292; AAK14912.1; -; mRNA.
DR   EMBL; AY358669; AAQ89032.1; -; mRNA.
DR   EMBL; DQ496109; ABF47098.1; -; Genomic_DNA.
DR   EMBL; AD000684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020612; AAH20612.1; -; mRNA.
DR   CCDS; CCDS12454.1; -.
DR   RefSeq; NP_066998.1; NM_021175.3.
DR   PDB; 1M4E; NMR; -; A=65-84.
DR   PDB; 1M4F; NMR; -; A=60-84.
DR   PDB; 2KEF; NMR; -; A=60-84.
DR   PDB; 3H0T; X-ray; 1.89 A; C=60-84.
DR   PDB; 4QAE; X-ray; 2.10 A; P/Q/R/S/T/U=60-84.
DR   PDB; 6WBV; EM; 2.50 A; B=60-84.
DR   PDBsum; 1M4E; -.
DR   PDBsum; 1M4F; -.
DR   PDBsum; 2KEF; -.
DR   PDBsum; 3H0T; -.
DR   PDBsum; 4QAE; -.
DR   PDBsum; 6WBV; -.
DR   AlphaFoldDB; P81172; -.
DR   EMDB; EMD-21599; -.
DR   SMR; P81172; -.
DR   BioGRID; 121776; 3.
DR   IntAct; P81172; 2.
DR   STRING; 9606.ENSP00000471894; -.
DR   BindingDB; P81172; -.
DR   ChEMBL; CHEMBL3989381; -.
DR   DrugBank; DB13257; Ferrous sulfate anhydrous.
DR   TCDB; 8.A.37.1.2; the hepcidin (hepcidin) family.
DR   PhosphoSitePlus; P81172; -.
DR   BioMuta; HAMP; -.
DR   DMDM; 10720397; -.
DR   jPOST; P81172; -.
DR   MassIVE; P81172; -.
DR   PaxDb; 9606-ENSP00000471894; -.
DR   PeptideAtlas; P81172; -.
DR   ProteomicsDB; 57692; -.
DR   ABCD; P81172; 4 sequenced antibodies.
DR   Antibodypedia; 29325; 487 antibodies from 30 providers.
DR   DNASU; 57817; -.
DR   Ensembl; ENST00000222304.5; ENSP00000222304.2; ENSG00000105697.9.
DR   Ensembl; ENST00000598398.5; ENSP00000471894.1; ENSG00000105697.9.
DR   GeneID; 57817; -.
DR   KEGG; hsa:57817; -.
DR   MANE-Select; ENST00000222304.5; ENSP00000222304.2; NM_021175.4; NP_066998.1.
DR   UCSC; uc002nyw.4; human.
DR   AGR; HGNC:15598; -.
DR   CTD; 57817; -.
DR   DisGeNET; 57817; -.
DR   GeneCards; HAMP; -.
DR   GeneReviews; HAMP; -.
DR   HGNC; HGNC:15598; HAMP.
DR   HPA; ENSG00000105697; Tissue enriched (liver).
DR   MalaCards; HAMP; -.
DR   MIM; 606464; gene.
DR   MIM; 613313; phenotype.
DR   neXtProt; NX_P81172; -.
DR   OpenTargets; ENSG00000105697; -.
DR   Orphanet; 648581; Digenic hemochromatosis.
DR   Orphanet; 79230; HJV or HAMP-related hemochromatosis.
DR   PharmGKB; PA29182; -.
DR   VEuPathDB; HostDB:ENSG00000105697; -.
DR   eggNOG; ENOG502T0FU; Eukaryota.
DR   GeneTree; ENSGT00390000003154; -.
DR   HOGENOM; CLU_2557737_0_0_1; -.
DR   InParanoid; P81172; -.
DR   OMA; PICLFCC; -.
DR   OrthoDB; 4846842at2759; -.
DR   PhylomeDB; P81172; -.
DR   TreeFam; TF330932; -.
DR   PathwayCommons; P81172; -.
DR   SignaLink; P81172; -.
DR   SIGNOR; P81172; -.
DR   BioGRID-ORCS; 57817; 318 hits in 1153 CRISPR screens.
DR   EvolutionaryTrace; P81172; -.
DR   GeneWiki; HAMP; -.
DR   GenomeRNAi; 57817; -.
DR   Pharos; P81172; Tbio.
DR   PRO; PR:P81172; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P81172; Protein.
DR   Bgee; ENSG00000105697; Expressed in right lobe of liver and 164 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; TAS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IDA:CACAO.
DR   GO; GO:0034755; P:iron ion transmembrane transport; IEA:Ensembl.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR   GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IMP:BHF-UCL.
DR   GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR   GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:1904479; P:negative regulation of intestinal absorption; IMP:BHF-UCL.
DR   GO; GO:0034760; P:negative regulation of iron ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR   GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR   GO; GO:0010039; P:response to iron ion; IMP:BHF-UCL.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR   InterPro; IPR010500; Hepcidin.
DR   PANTHER; PTHR16877; HEPCIDIN; 1.
DR   PANTHER; PTHR16877:SF0; HEPCIDIN; 1.
DR   Pfam; PF06446; Hepcidin; 1.
DR   Genevisible; P81172; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disease variant; Disulfide bond; Fungicide; Hormone; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..54
FT                   /id="PRO_0000013378"
FT   PEPTIDE         60..84
FT                   /note="Hepcidin-25"
FT                   /id="PRO_0000013379"
FT   PEPTIDE         65..84
FT                   /note="Hepcidin-20"
FT                   /id="PRO_0000013380"
FT   DISULFID        66..82
FT                   /evidence="ECO:0000269|PubMed:19553669"
FT   DISULFID        69..72
FT                   /evidence="ECO:0000269|PubMed:19553669"
FT   DISULFID        70..78
FT                   /evidence="ECO:0000269|PubMed:19553669"
FT   DISULFID        73..81
FT                   /evidence="ECO:0000269|PubMed:19553669"
FT   VARIANT         59
FT                   /note="R -> G (in HFE2B; dbSNP:rs779021719)"
FT                   /evidence="ECO:0000269|PubMed:14670915"
FT                   /id="VAR_042512"
FT   VARIANT         70
FT                   /note="C -> R (in HFE2B; dbSNP:rs1374259518)"
FT                   /evidence="ECO:0000269|PubMed:14630809"
FT                   /id="VAR_042513"
FT   VARIANT         71
FT                   /note="G -> D (in HFE2B; dbSNP:rs104894696)"
FT                   /evidence="ECO:0000269|PubMed:12915468,
FT                   ECO:0000269|PubMed:14633868, ECO:0000269|PubMed:14670915"
FT                   /id="VAR_026648"
FT   VARIANT         78
FT                   /note="C -> Y (in HFE2B; dbSNP:rs1462013476)"
FT                   /evidence="ECO:0000269|PubMed:15099344"
FT                   /id="VAR_042514"
FT   CONFLICT        31
FT                   /note="T -> M (in Ref. 3; AAK14912)"
FT                   /evidence="ECO:0000305"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:3H0T"
FT   STRAND          76..82
FT                   /evidence="ECO:0007829|PDB:3H0T"
SQ   SEQUENCE   84 AA;  9408 MW;  5F8DCA23D19D29F7 CRC64;
     MALSSQIWAA CLLLLLLLAS LTSGSVFPQQ TGQLAELQPQ DRAGARASWM PMFQRRRRRD
     THFPICIFCC GCCHRSKCGM CCKT
//